Incorporation of Pseudoproline Derivatives Allows the Facile Synthesis of Human IAPP, a Highly Amyloidogenic and Aggregation-Prone Polypeptide-Reference-Cited by-同舟云学术

Incorporation of Pseudoproline Derivatives Allows the Facile Synthesis of Human IAPP, a Highly Amyloidogenic and Aggregation-Prone Polypeptide

Published:2005-01-27 Issue:4 Volume:7 Page:693-696
ISSN:1523-7060
Container-title:Organic Letters
language:en
Short-container-title:Org. Lett.

Author:

Abedini Andisheh¹,Raleigh Daniel P.¹

Affiliation:

1. Department of Chemistry, Graduate Program in Biochemistry and Structural Biology, Graduate Program in Biophysics, State University of New York at Stony Brook, Stony Brook, New York 11794-3400

Publisher

American Chemical Society (ACS)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/ol047480%2B

Reference12 articles.

1. Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells.

2. ISLET AMYLOID FORMED FROM DIABETES-ASSOCIATED PEPTIDE MAY BE PATHOGENIC IN TYPE-2 DIABETES

3. Plasma islet amyloid polypeptide (Amylin) levels and their responses to oral glucose in Type 2 (non-insulin-dependent) diabetic patients

4. Effects of Meal Ingestion on Plasma Amylin Concentration in NIDDM and Nondiabetic Humans

5. Role of islet amyloid polypeptide secretion in insulin-resistant humans

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